PMID:18956885

Citation	Ryckelynck, M, Paulus, CA and Frugier, M (2008) Post-translational modifications guard yeast from misaspartylation. Biochemistry 47:12476-82
Abstract	Yeast aspartyl-tRNA synthetase (AspRS) is downregulated at the post-transcriptional level. This complex retro-inhibition mechanism causes the cell to equilibrate cellular concentrations of tRNAAsp, AspRS, and its encoding mRNA. This strategy hinders AspRS accumulation to keep misacylation of heterologous tRNAs under control. Here, the AspRS concentration was increased artificially in vivo but did not generate tRNAAsn and/or tRNAGlu misaspartylation or the logical consecutive post-translational stress. This work allowed the detection of an additional subtle cellular lock capable of blocking AspRS toxicity. This study revealed the presence of post-translational modifications in the N-terminal extension of AspRS. We hypothesize that by neutralizing the lysine-rich motif contained in this domain, the cell mobilizes an additional strategy that considerably reduces the probability of the enzyme binding and aspartylating noncognate tRNAs and thus harming its own translation.
Links	PubMed Online version:10.1021/bi8009295
Keywords	Amino Acid Sequence; Aminoacylation; Aspartate-tRNA Ligase/chemistry; Aspartate-tRNA Ligase/genetics; Aspartate-tRNA Ligase/metabolism; Aspartate-tRNA Ligase/toxicity; Aspartic Acid/metabolism; Biotin/metabolism; Gene Expression; Gentamicins/pharmacology; Glycosylation; Lysine/metabolism; Mass Spectrometry; Methylation; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Processing, Post-Translational; Proteome; Saccharomyces cerevisiae/cytology; Saccharomyces cerevisiae/drug effects; Saccharomyces cerevisiae/metabolism
edit table

Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status

References

See Help:References for how to manage references in GONUTS.